TRYPANOSOMA-BRUCEI-BRUCEI - ISOLATION OF THE MAJOR SURFACE COAT GLYCOPROTEIN BY LECTIN AFFINITY CHROMATOGRAPHY

We have purified soluble glycoproteins associated with Trypanosoma brucei brucei by lentil lectin affinity chromatography. The major surface coat glycoprotein (SCGp) accounts for 87% of the protein in the preparation with approximately 12 other glycoproteins accounting for the rest. This preparation can be further subdivided by DEAE chromatography. The nonabsorbed protein fraction is 95% SCGp and 1 to 2% each of three other glycoproteins. Elution of the DEAE column with a 0.05-0.5 M NaCl gradient yields a broad peak containing the remaining glycoproteins. The purification of the SCGp is 16- and 17.3-fold at each step out of a theoretical 18-fold possible purification. The preparation after lectin chromatography is stable, showing no degradation after standing 72 hr at 4 C. Additional purification procedures are discussed. © 1978.